ID   Q97IC3_CLOAB            Unreviewed;       269 AA.
AC   Q97IC3;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   04-NOV-2026, entry version 113.
DE   SubName: Full=Protein serine/threonine phosphatases, PP2C family (YLOO B.subtilis ortholog) {ECO:0000313|EMBL:AAK79693.1};
GN   OrderedLocusNames=CA_C1727 {ECO:0000313|EMBL:AAK79693.1};
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM
OS   19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79693.1, ECO:0000313|Proteomes:UP000000814};
RN   [1] {ECO:0000313|EMBL:AAK79693.1, ECO:0000313|Proteomes:UP000000814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC   {ECO:0000313|Proteomes:UP000000814};
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PROSITE-ProRule:PRU01082};
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DR   EMBL; AE001437; AAK79693.1; -; Genomic_DNA.
DR   PIR; B97113; B97113.
DR   AlphaFoldDB; Q97IC3; -.
DR   STRING; 272562.CA_C1727; -.
DR   KEGG; cac:CA_C1727; -.
DR   PATRIC; fig|272562.8.peg.1929; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   OMA; AACIMGK; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   NCBIfam; NF033484; Stp1_PP2C_phos; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   PANTHER; PTHR13832:SF860; PROTEIN PHOSPHATASE PHPP; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT   DOMAIN          22..259
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   269 AA;  29557 MW;  00DB9D5C66FEBC43 CRC64;
     MPLVDSLEEI ILKKVKGNNM KMVGMLSDIG TVRKLNEDYV GYYENDDIRF YVVADGMGGH
     NAGEVASKLA VDSTVKYIKE INNINLYELG DVLSSAIKFA NEQIYRKSKA SDGLSGMGTT
     ITACLIKDKD AVVANVGDSS CYFIKRDDII KITKDHSLVQ QLVDNGTITE KEALSHPNKN
     IITRALGTGE DVDVDIFDVT LNDVSKGILA TDGLTNVVDT REIYNIVLEN DNMVACQKLI
     ELSKDKGSRD NISVIVFEGE CKDDRNCAK
//